ID A0A0F7KRW1_9SPHN Unreviewed; 458 AA.
AC A0A0F7KRW1;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Argininosuccinate lyase {ECO:0000256|ARBA:ARBA00012338, ECO:0000256|HAMAP-Rule:MF_00006};
DE Short=ASAL {ECO:0000256|HAMAP-Rule:MF_00006};
DE EC=4.3.2.1 {ECO:0000256|ARBA:ARBA00012338, ECO:0000256|HAMAP-Rule:MF_00006};
DE AltName: Full=Arginosuccinase {ECO:0000256|HAMAP-Rule:MF_00006};
GN Name=argH1 {ECO:0000313|EMBL:AKH42339.1};
GN Synonyms=argH {ECO:0000256|HAMAP-Rule:MF_00006};
GN ORFNames=WYH_01294 {ECO:0000313|EMBL:AKH42339.1};
OS Croceibacterium atlanticum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Croceibacterium.
OX NCBI_TaxID=1267766 {ECO:0000313|EMBL:AKH42339.1, ECO:0000313|Proteomes:UP000034392};
RN [1] {ECO:0000313|EMBL:AKH42339.1, ECO:0000313|Proteomes:UP000034392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=26DY36 {ECO:0000313|EMBL:AKH42339.1,
RC ECO:0000313|Proteomes:UP000034392};
RA Wu Y.-H., Cheng H., Wu X.-W.;
RT "The complete genome of Altererythrobacter atlanticus strain 26DY36.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(N(omega)-L-arginino)succinate = fumarate + L-arginine;
CC Xref=Rhea:RHEA:24020, ChEBI:CHEBI:29806, ChEBI:CHEBI:32682,
CC ChEBI:CHEBI:57472; EC=4.3.2.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000985, ECO:0000256|HAMAP-
CC Rule:MF_00006};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine
CC from L-ornithine and carbamoyl phosphate: step 3/3.
CC {ECO:0000256|ARBA:ARBA00004941, ECO:0000256|HAMAP-Rule:MF_00006}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00006}.
CC -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00006}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP011452; AKH42339.1; -; Genomic_DNA.
DR RefSeq; WP_046904880.1; NZ_JACIJL010000001.1.
DR AlphaFoldDB; A0A0F7KRW1; -.
DR STRING; 1267766.WYH_01294; -.
DR KEGG; aay:WYH_01294; -.
DR PATRIC; fig|1267766.3.peg.1304; -.
DR OrthoDB; 9769623at2; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000034392; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004056; F:argininosuccinate lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IEA:InterPro.
DR CDD; cd01359; Argininosuccinate_lyase; 1.
DR Gene3D; 1.10.40.30; Fumarase/aspartase (C-terminal domain); 1.
DR Gene3D; 1.20.200.10; Fumarase/aspartase (Central domain); 1.
DR Gene3D; 1.10.275.10; Fumarase/aspartase (N-terminal domain); 1.
DR HAMAP; MF_00006; Arg_succ_lyase; 1.
DR InterPro; IPR029419; Arg_succ_lyase_C.
DR InterPro; IPR009049; Argininosuccinate_lyase.
DR InterPro; IPR024083; Fumarase/histidase_N.
DR InterPro; IPR020557; Fumarate_lyase_CS.
DR InterPro; IPR000362; Fumarate_lyase_fam.
DR InterPro; IPR022761; Fumarate_lyase_N.
DR InterPro; IPR008948; L-Aspartase-like.
DR NCBIfam; TIGR00838; argH; 1.
DR PANTHER; PTHR43814; ARGININOSUCCINATE LYASE; 1.
DR PANTHER; PTHR43814:SF1; ARGININOSUCCINATE LYASE; 1.
DR Pfam; PF14698; ASL_C2; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR PRINTS; PR00145; ARGSUCLYASE.
DR PRINTS; PR00149; FUMRATELYASE.
DR SUPFAM; SSF48557; L-aspartase-like; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00006};
KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571, ECO:0000256|HAMAP-
KW Rule:MF_00006}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00006};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00006};
KW Reference proteome {ECO:0000313|Proteomes:UP000034392}.
FT DOMAIN 4..298
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 361..430
FT /note="Argininosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14698"
SQ SEQUENCE 458 AA; 49435 MW; C30BD5D177F137F0 CRC64;
MWGGRFAEGP SAIMREINAS IPFDKALWRQ DIAASKAHVA MLGACGIVSA EDAKTIDAGL
DKVAAEYEVD GVPEDWDLED IHMTTESRLA ELIGPVAGRL HTARSRNDQV ATDFRLWVRD
AMDQADAGLE ALQKALVTRA GEHADAIMPG FTHLQTAQPV TLGHHLMAYY EMIRRDRSRF
RDARARMNES PLGSAALAGT GFPIDREMTA QALGFDRPTD NSLDAVSDRD FALDYLQAAA
QCSVHLSRLA EEFVIWASQP FGFVRMPDTL STGSSIMPQK KNPDAAELVR GHAGRIVGCA
TALLVTMKGL PLAYSKDMQD DKPPVFEAAN LLSLSIAAMT GMVADATFRT DRMLQAAQLG
YATATDLADW LVREANIPFR EAHHITGAAV KLAENKGVAL EALSLDELQA IDPRVGEGVY
KALSVEASVA ARASHGGTAP EQVRKRVAAA RGELEMDG
//